X-ray Crystallography of tRNA recycling enzyme:substrate complex
Project/Area Number |
24770093
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Structural biochemistry
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Research Institution | Niigata University |
Principal Investigator |
ITO Kosuke 新潟大学, 自然科学系, 助教 (20502397)
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | tRNA再生酵素 / ペプチジルtRNA / 翻訳 / X線結晶構造解析 / tRNA再生 / リボソーム / ストール / 酵素基質複合体 |
Outline of Final Research Achievements |
tRNA recycling enzyme cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are produced by aborted translation, to recycle tRNA for further rounds of protein synthesis. Here we have determined the crystal structure of the tRNA recycling enzyme in complex with the tRNA CCA-acceptor-TΨC domain, the enzyme-binding region of the tRNA moiety of the substrate. The structure provided insights into how tRNA recycling enzyme accepts the diverse sequences of the elongator-tRNAs as substrate components. Furthermore, we proposed an authentic tRNA recycling enzyme:peptidyl-tRNA complex model, based on the present structure and the enzymatic studies’results.
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Report
(4 results)
Research Products
(23 results)
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[Journal Article] Molecular insights into the interaction of the ribosomal stalk protein with elongation factor 1α.2014
Author(s)
Ito, K., Honda, T., Suzuki, T., Miyoshi, T., Murakami, R., Yao, M., and Uchiumi T.
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Journal Title
Nucleic Acids Res.
Volume: 42
Issue: 22
Pages: 14042-14052
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Crystal structure of α-amylase from Oryza sativa molecular insights into enzyme activity and thermostability2014
Author(s)
Akihito OCHIAI, Hiroshi SUGAI, Kazuki HARADA, Seiya TANAKA, Yohei ISHIYAMA, Kosuke ITO, Takaaki TANAKA, Toshio UCHIUMI, Masayuki TANIGUCHI, Toshiaki MITSUI
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Journal Title
Bioscience, Biotechnology, and Biochemistry
Volume: in press
Related Report
Peer Reviewed
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[Journal Article] Solution structure of human P1-P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome2013
Author(s)
Lee, K.M., Yusa, K., Chu, L.O., Yu, C.W., Oono, M., Miyoshi, T., Ito, K., Shaw, P.C., Wong, K.B., and Uchiumi, T
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Journal Title
Nucleic Acids Res
Volume: 41
Issue: 18
Pages: 8776-8787
DOI
Related Report
Peer Reviewed
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